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3P48

Structure of the yeast dUTPase DUT1 in complex with dUMPNPP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004170molecular_functiondUTP diphosphatase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006226biological_processdUMP biosynthetic process
A0009117biological_processnucleotide metabolic process
A0009213biological_processpyrimidine deoxyribonucleoside triphosphate catabolic process
A0016787molecular_functionhydrolase activity
A0035863biological_processdITP catabolic process
A0035870molecular_functiondITP diphosphatase activity
A0046081biological_processdUTP catabolic process
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0004170molecular_functiondUTP diphosphatase activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006226biological_processdUMP biosynthetic process
B0009117biological_processnucleotide metabolic process
B0009213biological_processpyrimidine deoxyribonucleoside triphosphate catabolic process
B0016787molecular_functionhydrolase activity
B0035863biological_processdITP catabolic process
B0035870molecular_functiondITP diphosphatase activity
B0046081biological_processdUTP catabolic process
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0004170molecular_functiondUTP diphosphatase activity
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0006226biological_processdUMP biosynthetic process
C0009117biological_processnucleotide metabolic process
C0009213biological_processpyrimidine deoxyribonucleoside triphosphate catabolic process
C0016787molecular_functionhydrolase activity
C0035863biological_processdITP catabolic process
C0035870molecular_functiondITP diphosphatase activity
C0046081biological_processdUTP catabolic process
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE DUP A 148
ChainResidue
AARG68
AHOH186
AHOH211
AHOH246
AHOH247
AHOH260
AHOH406
CLYS74
CALA81
CGLY82
CVAL83
ASER69
CASP85
CTYR88
CLYS93
AGLY70
AGLN114
AMG149
AHOH164
AHOH168
AHOH176
AHOH178

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 149
ChainResidue
ADUP148
AHOH168
AHOH246
AHOH247

site_idAC3
Number of Residues23
DetailsBINDING SITE FOR RESIDUE DUP B 148
ChainResidue
AALA81
AGLY82
AVAL83
AASP85
ATYR88
AVAL92
ALYS93
BARG68
BSER69
BGLY70
BGLN114
BMG150
BHOH161
BHOH175
BHOH180
BHOH207
BHOH214
BHOH219
BHOH248
BHOH249
BHOH250
BHOH257
BHOH396

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE DUP B 149
ChainResidue
BALA81
BGLY82
BVAL83
BASP85
BTYR88
BVAL92
BLYS93
BHOH190
BHOH225
BHOH234
BHOH276
BHOH377
CMET48
CARG68
CSER69
CGLY70
CGLN114
CMG148

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 150
ChainResidue
BDUP148
BHOH248
BHOH249
BHOH250

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG C 148
ChainResidue
BDUP149
BHOH276
CASP32

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:21548881, ECO:0007744|PDB:3F4F
ChainResidueDetails
ASER69
BGLY82
BASP85
BTYR88
BLYS93
BARG137
BPHE142
BGLY143
CSER69
CGLY82
CASP85
AGLY82
CTYR88
CLYS93
CARG137
CPHE142
CGLY143
AASP85
ATYR88
ALYS93
AARG137
APHE142
AGLY143
BSER69

227344

PDB entries from 2024-11-13

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